The role of heat shock protein 70 in vitamin D receptor function

Ward Lutz, Kenji Kohno, Rajiv Kumar

Research output: Contribution to journalArticle

19 Citations (Scopus)

Abstract

We previously demonstrated that the 1α,25-dihydroxyvitamin D3 receptor (VDR) interacts with the constitutive heat shock protein, hsc70 in vitro, and with DnaK (Biochem. Biophys. Res. Commun. 260, 446-452, 1999). The biological significance of VDR-heat shock protein interactions, however, is unknown. To examine the role of such interactions in eukaryotic cells, we heterologously expressed VDR and RXRα together with a vitamin D-responsive reporter system in Saccharomyces cerevisiae and examined the consequences of heat shock protein 70 gene (SSA) deletion in these cells. We show that heterologously expressed VDR associates with the yeast cytosolic hsp70 protein, Ssa1p. Deletion of the SSA2, SSA3, and SSA4 genes and reduction of Ssa1p activity, reduces the intracellular concentrations of the VDR and its heterodimeric partner, RXRα and reduces the activity of a vitamin D-dependent gene. Hsp70-like chaperone proteins play a role in controlling concentrations of the VDR within the cell.

Original languageEnglish (US)
Pages (from-to)1211-1219
Number of pages9
JournalBiochemical and Biophysical Research Communications
Volume282
Issue number5
DOIs
StatePublished - 2001

Fingerprint

Calcitriol Receptors
HSP70 Heat-Shock Proteins
Genes
Heat-Shock Proteins
Vitamin D
Yeast
Gene Deletion
Eukaryotic Cells
Saccharomyces cerevisiae
Proteins
Yeasts

Keywords

  • Chaperones
  • Heat shock protein 70
  • Vitamin D receptor

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

The role of heat shock protein 70 in vitamin D receptor function. / Lutz, Ward; Kohno, Kenji; Kumar, Rajiv.

In: Biochemical and Biophysical Research Communications, Vol. 282, No. 5, 2001, p. 1211-1219.

Research output: Contribution to journalArticle

@article{fed6d072dc514b2598857d8f6310ba8c,
title = "The role of heat shock protein 70 in vitamin D receptor function",
abstract = "We previously demonstrated that the 1α,25-dihydroxyvitamin D3 receptor (VDR) interacts with the constitutive heat shock protein, hsc70 in vitro, and with DnaK (Biochem. Biophys. Res. Commun. 260, 446-452, 1999). The biological significance of VDR-heat shock protein interactions, however, is unknown. To examine the role of such interactions in eukaryotic cells, we heterologously expressed VDR and RXRα together with a vitamin D-responsive reporter system in Saccharomyces cerevisiae and examined the consequences of heat shock protein 70 gene (SSA) deletion in these cells. We show that heterologously expressed VDR associates with the yeast cytosolic hsp70 protein, Ssa1p. Deletion of the SSA2, SSA3, and SSA4 genes and reduction of Ssa1p activity, reduces the intracellular concentrations of the VDR and its heterodimeric partner, RXRα and reduces the activity of a vitamin D-dependent gene. Hsp70-like chaperone proteins play a role in controlling concentrations of the VDR within the cell.",
keywords = "Chaperones, Heat shock protein 70, Vitamin D receptor",
author = "Ward Lutz and Kenji Kohno and Rajiv Kumar",
year = "2001",
doi = "10.1006/bbrc.2001.4711",
language = "English (US)",
volume = "282",
pages = "1211--1219",
journal = "Biochemical and Biophysical Research Communications",
issn = "0006-291X",
publisher = "Academic Press Inc.",
number = "5",

}

TY - JOUR

T1 - The role of heat shock protein 70 in vitamin D receptor function

AU - Lutz, Ward

AU - Kohno, Kenji

AU - Kumar, Rajiv

PY - 2001

Y1 - 2001

N2 - We previously demonstrated that the 1α,25-dihydroxyvitamin D3 receptor (VDR) interacts with the constitutive heat shock protein, hsc70 in vitro, and with DnaK (Biochem. Biophys. Res. Commun. 260, 446-452, 1999). The biological significance of VDR-heat shock protein interactions, however, is unknown. To examine the role of such interactions in eukaryotic cells, we heterologously expressed VDR and RXRα together with a vitamin D-responsive reporter system in Saccharomyces cerevisiae and examined the consequences of heat shock protein 70 gene (SSA) deletion in these cells. We show that heterologously expressed VDR associates with the yeast cytosolic hsp70 protein, Ssa1p. Deletion of the SSA2, SSA3, and SSA4 genes and reduction of Ssa1p activity, reduces the intracellular concentrations of the VDR and its heterodimeric partner, RXRα and reduces the activity of a vitamin D-dependent gene. Hsp70-like chaperone proteins play a role in controlling concentrations of the VDR within the cell.

AB - We previously demonstrated that the 1α,25-dihydroxyvitamin D3 receptor (VDR) interacts with the constitutive heat shock protein, hsc70 in vitro, and with DnaK (Biochem. Biophys. Res. Commun. 260, 446-452, 1999). The biological significance of VDR-heat shock protein interactions, however, is unknown. To examine the role of such interactions in eukaryotic cells, we heterologously expressed VDR and RXRα together with a vitamin D-responsive reporter system in Saccharomyces cerevisiae and examined the consequences of heat shock protein 70 gene (SSA) deletion in these cells. We show that heterologously expressed VDR associates with the yeast cytosolic hsp70 protein, Ssa1p. Deletion of the SSA2, SSA3, and SSA4 genes and reduction of Ssa1p activity, reduces the intracellular concentrations of the VDR and its heterodimeric partner, RXRα and reduces the activity of a vitamin D-dependent gene. Hsp70-like chaperone proteins play a role in controlling concentrations of the VDR within the cell.

KW - Chaperones

KW - Heat shock protein 70

KW - Vitamin D receptor

UR - http://www.scopus.com/inward/record.url?scp=0034806815&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0034806815&partnerID=8YFLogxK

U2 - 10.1006/bbrc.2001.4711

DO - 10.1006/bbrc.2001.4711

M3 - Article

VL - 282

SP - 1211

EP - 1219

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

SN - 0006-291X

IS - 5

ER -